PubMed · 6725957
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A M Mastro. 1984. IgA release using phorbol?. https://pubmed.ncbi.nlm.nih.gov/6725957/
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Thirteen serovars of Ureaplasma urealyticum were analyzed for the ability to cleave human IgA. Strains of all of the serovars tested cleaved IgA 1 in the hinge region of the alpha-chain, resulting in intact Fc and monomeric Fab fragments. IgA 1 protease activity was also observed in concentrated cell-free extracts of spent cultivation medium, indicating that the IgA 1 protease was excreted into the medium during growth of the micro-organisms. Five clinical isolates of U. urealyticum obtained from urine, cervix, vagina, amniotic fluid, and synovial fluid were positive for IgA 1 protease activity. No proteolytic activity was observed against human IgA 2, IgG, or IgM. Strains of Mycoplasma fermentans, M. salivarium and seven serovars of M. hominis were negative for IgA 1 protease activity.
Human milk contains factors such as IgA and lactoferrin that increase the newborn infant's resistance to infection. Preterm infants are fed pooled milk, which is normally sterilised by heating. After standard heat sterilisation IgA and lactoferrin were undetectable in milk samples. Pasteurisation also sterilised milk samples even after heavy artificial contamination and did not damage the proteins. Gamma-irradiation sterilised equally effectively but caused some denaturation of IgA and lactoferrin. Since most of the milk samples were sterile or had only light contamination with skin bacteria, there seems to be no need for routine sterilisation. If sterilisation is necessary, the method used should be chosen to minimise damage to milk proteins.
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